纤溶酶和胰蛋白酶将C'IS转化为C'1酯酶。
The conversion of C'IS to C'1 esterase by plasmin and trypsin.
作者信息
Ratnoff O D, Naff G B
出版信息
J Exp Med. 1967 Feb 1;125(2):337-58. doi: 10.1084/jem.125.2.337.
Abstract
The formation of C'1 esterase from C'1, the first component of complement, may be brought about by the action of plasmin or trypsin upon C'1s, a subcomponent of C'1. These enzymes also decrease the esterolytic activity of C'1 esterase. The formation of C'1 esterase was demonstrated by measuring the appearance of an agent or agents with esterolytic properties and the capacity to inactivate C'2 and C'4, attributes of C'1 esterase. The activity of the agent which evolved was blocked by serum inhibitor of C'1 esterase. The implications of these observations, that the formation of C'1 esterase during complement fixation is mediated by proteolytic processes, are under study. The possible inhibition of C'1q by soybean trypsin inhibitor is in agreement with this hypothesis.
摘要
补体的首个成分C'1可通过纤溶酶或胰蛋白酶作用于C'1的一个亚成分C'1s而形成C'1酯酶。这些酶还会降低C'1酯酶的酯解活性。通过测量具有酯解特性及使C'2和C'4失活能力（C'1酯酶的特性）的一种或多种物质的出现来证实C'1酯酶的形成。所产生物质的活性被C'1酯酶的血清抑制剂所阻断。关于补体固定过程中C'1酯酶的形成由蛋白水解过程介导这一观察结果的意义正在研究之中。大豆胰蛋白酶抑制剂对C'1q的可能抑制作用与这一假说相符。
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